ArticleExtremophiles : life under extreme conditions2016
A high-molecular-weight, alkaline, and thermostable β-1,4-xylanase of a subseafloor Microcella alkaliphila.
Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- High-Molecular-Weight Xylanase from B. pumilus US570 Strain: Purification, Characterization and Application in Banana and Orange Peels Hydrolysis and Breadmaking.Applied biochemistry and biotechnology · 2024Article
- Review
- Xylanolytic Extremozymes Retrieved From Environmental Metagenomes: Characteristics, Genetic Engineering, and Applications.Frontiers in microbiology · 2020Review
- A New Group of Modular Xylanases in Glycoside Hydrolase Family 8 from Marine Bacteria.Applied and environmental microbiology · 2018Article
- A Novel Multi-domain High Molecular, Salt-Stable Alkaline Xylanase fromFrontiers in microbiology · 2016Article
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Authors and funding
9 authors.
Funding
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Abstract
An endo β-1,4-xylanase (XynE15) from a culture broth of a deep subseafloor microorganism, Microcella alkaliphila JAM-AC0309, was purified to homogeneity. The molecular mass of XynE15 was approximately 150 kDa as judged by SDS-PAGE. The optimal pH and temperature for hydrolysis of xylan were pH 8 and 65 °C. The enzyme was stable to incubation for 30 min at up to 75 °C, and the half-life at 50 °C was 48 h. XynE15 hydrolyzed arabinoxylan, oat spelt xylan, and birchwood xylan well, but not avicel, carboxymethylcellulose, or arabinan. Xylooligosaccharides were hydrolyzed to mainly xylobiose from higher than xylotetraose. The genome sequencing analysis of strain JAM-AC03039 revealed that XynE15 was composed of 1,319 amino acids with one catalytic domain and three carbohydrate-binding domains belonging to glycoside hydrolase (GH) family 10 and carbohydrate-binding module (CBM) family 4, respectively.
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Registered trials
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